User:Mbennie/Notebook/Papers and Books/IgA Autotransporter

Error fetching PMID 12949111

• Fused leucine zipper with autotransporter creating a protein that was expressed on the cell surface and adhered to a similar protein expressed in another population of cells, causing the cells to clump out of solution
• Used IgA as the AT
• Used Fos and Jun as the leucine zippers
• Used an E-tag to test whether the protein was expressed on the surface (using an antibody)
• Used pelB "for an efficient secretion"
• Membrane remains stable

Error fetching PMID 8254661

• Concludes a subset of IgA (882 bp) can transport and display a passenger protein by itself, called Iga beta-core
• Figured out that Iga beta was enough, then kept cutting up the protein was no longer functional
• This 227aa protein is very well conserved among Neisseria and Haemophilus
• p. 583 - protein sequence of Iga beta-core
• Suggests that cell express 50,000-100,000 copies
• Iga beta-core is "structurally reminiscent of integral outer membrane proteins (OMPs)"
• Suggests further that forty of the amino acids might not be needed (p. 590)
• "Resembles a typical outer membrane protein with a few additional features"

Error fetching PMID 10835606

• Describes method of bioremediation using r. eutropha using metallothionein (MT) expressed on the cellular surface using IgA beta
• MT binds heavy metal atoms
• Bioaccumulates about 5% of Cd2+ ions tested, but affects the growth of plants in contaminated soil much more (70%)

Error fetching PMID 2189728

• Discovery that IgA beta contains the ability to display surface proteins by itself
• Observation that there is a highly conserved region within IgA beta, called IgA beta-core, which is the portion that facilitates outer membrane transport
• Observed that disulphide-dependent folding can cause problems in surface display (protein stuck in periplasm)

Error fetching PMID 3027577

• A basic description of IgA protein in Neisseria gonorrhoeae

Error fetching PMID 10510237

• It is possible to have disulfide-dependent folding, but it decreases efficiency (3-fold with Fv)

Error fetching PMID 15014442

• Resolves crystal structure of N. meningitidis IgA (highly homologous to N. gonorrhoeae IgA)
• "12-stranded beta-barrel with a hydrophilic pore of 10*12.5 A that is filled by an N-terminus alpha-helix"
• Evidence supporting passenger-domain transport, evidence against oligomer of translocater domains
• Alpha-helix has many interactions with interior of hydrophilic barrel: seven salt bridges, sixteen hydrogen bonds, and numerous van der Waals contacts
• Deletion of alpha-helix results in much lower expression of the protein, but increased pore activity